Summary for 3PSG
| Entry DOI | 10.2210/pdb3psg/pdb |
| Descriptor | PEPSINOGEN (2 entities in total) |
| Functional Keywords | hydrolase(acid proteinase zymogen) |
| Biological source | Sus scrofa (pig) |
| Cellular location | Secreted: P00791 |
| Total number of polymer chains | 1 |
| Total formula weight | 39551.52 |
| Authors | Hartsuck, J.A.,Koelsch, G.,Remington, S.J. (deposition date: 1991-09-03, release date: 1993-01-15, Last modification date: 2024-11-20) |
| Primary citation | Hartsuck, J.A.,Koelsch, G.,Remington, S.J. The high-resolution crystal structure of porcine pepsinogen. Proteins, 13:1-25, 1992 Cited by PubMed Abstract: The structure of porcine pepsinogen at pH 6.1 has been refined to an R-factor of 0.173 for data extending to 1.65 A. The final model contains 180 solvent molecules and lacks density for residues 157-161. The structure of this aspartic proteinase zymogen possesses many of the characteristics of pepsin, the mature enzyme. The secondary structure of the zymogen consists predominantly of beta-sheet, with an approximate 2-fold axis of symmetry. The activation peptide packs into the active site cleft, and the N-terminus (1P-9P) occupies the position of the mature N-terminus (1-9). Thus changes upon activation include excision of the activation peptide and proper relocation of the mature N-terminus. The activation peptide or residues of the displaced mature N-terminus make specific interactions with the substrate binding subsites. The active site of pepsinogen is intact; thus the lack of activity of pepsinogen is not due to a deformation of the active site. Nine ion pairs in pepsinogen may be important in the advent of activation and involve the activation peptide or regions of the mature N-terminus which are relocated in the mature enzyme. The activation peptide-pepsin junction, 44P-1, is characterized by high thermal parameters and weak density, indicating a flexible structure which would be accessible to cleavage. Pepsinogen is an appropriate model for the structures of other zymogens in the aspartic proteinase family. PubMed: 1594574DOI: 10.1002/prot.340130102 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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